ID   E7EX57_HUMAN            Unreviewed;       443 AA.
AC   E7EX57;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Multidrug and toxin extrusion protein 1 {ECO:0000256|ARBA:ARBA00040218};
DE   AltName: Full=Solute carrier family 47 member 1 {ECO:0000256|ARBA:ARBA00042671};
GN   Name=SLC47A1 {ECO:0000313|Ensembl:ENSP00000407155.2};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000407155.2, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000407155.2, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [2] {ECO:0007829|PubMed:22814378}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [3] {ECO:0000313|Ensembl:ENSP00000407155.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + thiamine(out) = H(+)(out) + thiamine(in);
CC         Xref=Rhea:RHEA:71271, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385;
CC         Evidence={ECO:0000256|ARBA:ARBA00036230};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=agmatine(in) + H(+)(out) = agmatine(out) + H(+)(in);
CC         Xref=Rhea:RHEA:72127, ChEBI:CHEBI:15378, ChEBI:CHEBI:58145;
CC         Evidence={ECO:0000256|ARBA:ARBA00036531};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72128;
CC         Evidence={ECO:0000256|ARBA:ARBA00036531};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:72129;
CC         Evidence={ECO:0000256|ARBA:ARBA00036531};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=creatinine(in) + H(+)(out) = creatinine(out) + H(+)(in);
CC         Xref=Rhea:RHEA:72183, ChEBI:CHEBI:15378, ChEBI:CHEBI:16737;
CC         Evidence={ECO:0000256|ARBA:ARBA00036975};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=estrone 3-sulfate(in) + H(+)(out) = estrone 3-sulfate(out) +
CC         H(+)(in); Xref=Rhea:RHEA:72139, ChEBI:CHEBI:15378, ChEBI:CHEBI:60050;
CC         Evidence={ECO:0000256|ARBA:ARBA00035934};
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004424}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE)
CC       (TC 2.A.66.1) family. {ECO:0000256|ARBA:ARBA00010199}.
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DR   EMBL; AC004448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC025627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; E7EX57; -.
DR   SMR; E7EX57; -.
DR   MassIVE; E7EX57; -.
DR   MaxQB; E7EX57; -.
DR   PeptideAtlas; E7EX57; -.
DR   ProteomicsDB; 18988; -.
DR   Antibodypedia; 13691; 169 antibodies from 30 providers.
DR   Ensembl; ENST00000436810.6; ENSP00000407155.2; ENSG00000142494.13.
DR   UCSC; uc010vyz.2; human.
DR   HGNC; HGNC:25588; SLC47A1.
DR   VEuPathDB; HostDB:ENSG00000142494; -.
DR   GeneTree; ENSGT00940000161644; -.
DR   HOGENOM; CLU_012893_1_3_1; -.
DR   ChiTaRS; SLC47A1; human.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000142494; Expressed in right adrenal gland cortex and 152 other cell types or tissues.
DR   ExpressionAtlas; E7EX57; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR   GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
DR   CDD; cd13132; MATE_eukaryotic; 1.
DR   InterPro; IPR045069; MATE_euk.
DR   InterPro; IPR002528; MATE_fam.
DR   NCBIfam; TIGR00797; matE; 1.
DR   PANTHER; PTHR11206:SF73; MULTIDRUG AND TOXIN EXTRUSION PROTEIN 1; 1.
DR   PANTHER; PTHR11206; MULTIDRUG RESISTANCE PROTEIN; 1.
DR   Pfam; PF01554; MatE; 2.
PE   1: Evidence at protein level;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:E7EX57,
KW   ECO:0007829|ProteomicsDB:E7EX57};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        37..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        133..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        194..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        274..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        315..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        355..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        391..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   443 AA;  48027 MW;  5255E025EFD592F2 CRC64;
     MEAPEEPAPV RGGPEATLEV RGSRCLRLSA FREELRALLV LAGPAFLVQL MVFLISFISS
     VFCGHLGKLE LDAVTLAIAT YGSQNLKHVG VILQRSALVL LLCCFPCWAL FLNTQHILLL
     FRQDPDVSRL TQTYVTIFIP ALPATFLYML QVKYLLNQGI VLPQIVTGVA ANLVNALANY
     LFLHQLHLGV IGSALANLIS QYTLALLLFL YILGKKLHQA TWGGWSLECL QDWASFLRLA
     IPSMLMLCME WWAYEVGSFL SGILGMVELG AQSIVYELAI IVYMVPAGFS VAASVRVGNA
     LGAGDMEQAR KSSTVSLLIT VLFAVAFSVL LLSCKDHVGY IFTTDRDIIN LVAQVVPIYA
     VSHLFEALAC TSGGVLRGSG NQKVGAIVNT IGYYVVGLPI GIALMFATTL GVMGSGTRQF
     ESKQRASEWE FCSPSGSASP RVP
//